Publication | Closed Access
The Mechanism of Class II, Metal‐Dependent Aldolases
107
Citations
30
References
1996
Year
Molecular PharmacologyClass IiZn2+-dependent AldolasesBiochemistryCellular EnzymologyNatural SciencesMedicineEnzyme CatalysisMolecular BiologyCc BondStructure-function Enzyme KineticsChemical BiologyModel CompoundsMolecular ModelingRedox Biology
Chelation of the cis-enediolate form of dihydroxyacetone phosphate (see picture on the right) is the key step in the mechanism of action of Zn2+-dependent aldolases. This proposal is derived from inhibition studies with model compounds for both ground and transition states and from an X-ray structure determination of a protein—ligand complex. The high degree of asymmetric induction occurring at both termini of the newly formed CC bond can now be explained.
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